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Streptavidin-biotin complex, pH 2.40, space group I222

Analyse Streptavidin-biotin complex, pH 2.40, space group I222 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2RTG
Type: protein
Length: 244 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Streptavidin
UniProt: P22629
Ligands: BTN, CL, SO4
Pockets: 3 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Streptavidin	protein	123	6% helix, 55% strand	P22629
D	Streptavidin	protein	121	5% helix, 55% strand	P22629

Ligands and binding sites

BTN · Biotin · ligand · 2 copies · chains B, D
CL · Chloride ion · ion · chains B
SO4 · Sulfate ion · ion · chains D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	89	0.46	0.80	17	BTN
2	89	0.45	0.80	17	BTN
3	61	0.30	0.76	21	empty

Interfaces

1 interface between chains.

B–D · 1593 Å² buried · 31 hydrogen bonds · protein-protein

Compared structures

2RTG · Streptavidin-biotin complex, pH 2.40, space group I222 · the same entry in another collection · chain B against B, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P22629
Elsewhere: RCSB PDB 2RTG · PDBe 2RTG · UniProt P22629

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